2QEL

Crystal structure of the highly amyloidogenic transthyretin mutant TTR G53S/E54D/L55S- heated protein

Summary for 2QEL

• Entry DOI: 10.2210/pdb2qel/pdb
• Related: 1g1o
• Descriptor: Transthyretin (2 entities in total)
• Functional Keywords: greek key, beta barrel, beta-slip, protein heating, transport protein
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P02766
• Total number of polymer chains: 4
• Total formula weight: 55069.12

Authors

Karlsson, A.,Sauer-Eriksson, A.E. (deposition date: 2007-06-26, release date: 2007-09-04, Last modification date: 2023-08-30)

Primary citation

Karlsson, A.,Sauer-Eriksson, A.E.
Heating of proteins as a means of improving crystallization: a successful case study on a highly amyloidogenic triple mutant of human transthyretin
Acta Crystallogr.,Sect.F, 63:695-700, 2007

PubMed Abstract: The use of high temperatures in the purification procedures of heat-stable proteins is a well established technique. Recently, rapid pre-heat treatment of protein samples prior to crystallization trials was described as a final polishing step to improve the diffraction properties of crystals [Pusey et al. (2005), Prog. Biophys. Mol. Biol. 88, 359-386]. The present study demonstrates that extended high-temperature incubation (328 K for 48 h) of the highly amyloidogenic transthyretin mutant TTR G53S/E54D/L55S successfully removes heterogeneities and allows the reproducible growth of well diffracting crystals. Heat treatment might be applied as an optimization method to other cases in which the protein/biomolecule fails to form diffracting crystals.

PubMed: 17671371
DOI: 10.1107/S1744309107033957

Experimental method

X-RAY DIFFRACTION (2.29 Å)